Treatment with crystalline ultra-pure urea reduces the aggregation of integral membrane proteins without inhibiting N-terminal sequencing

Journal of Biochemistry

Volumn 124, Issue 2, 1998, Pages 417-420

  Soulié, Stéphanie ^a   Denoroy, Luc ^b,e   Le Caer, Jean Pierre ^b   Hamasaki, Naotaka ^c   Groves, Jonathan D ^d   Le Maire, Marc ^a  

^a CEA SACLAY   (France)

^b CNRS   (France)

^c KYUSHU UNIVERSITY   (Japan)

^d UNIVERSITY OF BRISTOL   (United Kingdom)

^e UNIVERSITÉ LYON 1   (France)

Author keywords

Carbamylation; Membrane protein; N terminal sequencing; Topology; Urea

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ANAZOLENE SODIUM; FLUORIDE; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; MYOGLOBIN; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; HYDROPHOBICITY; MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN AGGREGATION; PROTEIN DEGRADATION;

EID: 0031656620     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022128     Document Type: Article

References (13)

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